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Diacylglycerol mediates regulation of TASK potassium channels by Gq-coupled receptors

Author

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  • Bettina U. Wilke

    (Institute of Physiology and Pathophysiology, Philipps University)

  • Moritz Lindner

    (Institute of Physiology and Pathophysiology, Philipps University
    Present address: Department of Ophthalmology, University of Bonn, Bonn, Germany)

  • Lea Greifenberg

    (Institute of Physiology and Pathophysiology, Philipps University)

  • Alexandra Albus

    (Institute of Physiology and Pathophysiology, Philipps University)

  • Yannick Kronimus

    (Institute of Physiology and Pathophysiology, Philipps University)

  • Moritz Bünemann

    (Philipps University)

  • Michael G. Leitner

    (Institute of Physiology and Pathophysiology, Philipps University)

  • Dominik Oliver

    (Institute of Physiology and Pathophysiology, Philipps University)

Abstract

The two-pore domain potassium (K2P) channels TASK-1 (KCNK3) and TASK-3 (KCNK9) are important determinants of background K+ conductance and membrane potential. TASK-1/3 activity is regulated by hormones and transmitters that act through G protein-coupled receptors (GPCR) signalling via G proteins of the Gαq/11 subclass. How the receptors inhibit channel activity has remained unclear. Here, we show that TASK-1 and -3 channels are gated by diacylglycerol (DAG). Receptor-initiated inhibition of TASK required the activity of phospholipase C, but neither depletion of the PLC substrate PI(4,5)P2 nor release of the downstream messengers IP3 and Ca2+. Attenuation of cellular DAG transients by DAG kinase or lipase suppressed receptor-dependent inhibition, showing that the increase in cellular DAG—but not in downstream lipid metabolites—mediates channel inhibition. The findings identify DAG as the signal regulating TASK channels downstream of GPCRs and define a novel role for DAG that directly links cellular DAG dynamics to excitability.

Suggested Citation

  • Bettina U. Wilke & Moritz Lindner & Lea Greifenberg & Alexandra Albus & Yannick Kronimus & Moritz Bünemann & Michael G. Leitner & Dominik Oliver, 2014. "Diacylglycerol mediates regulation of TASK potassium channels by Gq-coupled receptors," Nature Communications, Nature, vol. 5(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms6540
    DOI: 10.1038/ncomms6540
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    Cited by:

    1. Yoshiaki Suzuki & Kanako Tsutsumi & Tatsuya Miyamoto & Hisao Yamamura & Yuji Imaizumi, 2017. "Heterodimerization of two pore domain K+ channel TASK1 and TALK2 in living heterologous expression systems," PLOS ONE, Public Library of Science, vol. 12(10), pages 1-17, October.
    2. Susanne Rinné & Florian Schick & Kirsty Vowinkel & Sven Schütte & Cornelius Krasel & Silke Kauferstein & Martin K.-H. Schäfer & Aytug K. Kiper & Thomas Müller & Niels Decher, 2024. "Potassium channel TASK-5 forms functional heterodimers with TASK-1 and TASK-3 to break its silence," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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